3SGB

STRUCTURE OF THE COMPLEX OF STREPTOMYCES GRISEUS PROTEASE B AND THE THIRD DOMAIN OF THE TURKEY OVOMUCOID INHIBITOR AT 1.8 ANGSTROMS RESOLUTION

Replaces:  2SGBReplaces:  1SGB

Functional Information from GO Data

Chain	GOid	namespace	contents
E	0004252	molecular_function	serine-type endopeptidase activity
E	0006508	biological_process	proteolysis
I	0004867	molecular_function	serine-type endopeptidase inhibitor activity

Functional Information from PROSITE/UniProt

site_id	PS00134
Number of Residues	6
Details	TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAGHC

Chain	Residue	Details
E	LEU53-CYS58

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site_id	PS00135
Number of Residues	12
Details	TRYPSIN_SER Serine proteases, trypsin family, serine active site. CAepGDSGGPLY

Chain	Residue	Details
E	CYS191-TYR200

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site_id	PS00282
Number of Residues	23
Details	KAZAL_1 Kazal serine protease inhibitors family signature. CtleyRplCgSdnktYgnkCnf.C

Chain	Residue	Details
I	CYS16-CYS38

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	SITE: Reactive bond 3 for chymotrypsin, elastase, proteases A and B, and subtilisin

Chain	Residue	Details
I	LEU18
E	ASP102
E	SER195

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site_id	SWS_FT_FI2
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine

Chain	Residue	Details
I	ASN45

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1ssx

Chain	Residue	Details
E	ASP102
E	SER195
E	GLY193
E	HIS57

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site_id	CSA2
Number of Residues	5
Details	Annotated By Reference To The Literature 1ssx

Chain	Residue	Details
E	ASP102
E	SER195
E	GLY193
E	HIS57
E	SER214

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site_id	MCSA1
Number of Residues	5
Details	M-CSA 608

Chain	Residue	Details
E	HIS57	proton acceptor, proton donor
E	ASP102	electrostatic stabiliser
E	GLY193	electrostatic stabiliser
E	SER195	nucleofuge, nucleophile, proton acceptor, proton donor
E	SER214	electrostatic stabiliser

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